• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


Phosphorylation of Fanconi anemia protein, FANCA, is regulated by Akt kinase.

Phosphorylation of the Fanconi anemia complementation group A (FANCA) protein is thought to be important for the function of the FA pathway. However, the kinase for FANCA (so-called FANCA-PK) remains to be identified. FANCA has a consensus sequence for Akt kinase near serine 1149 (Ser1149), suggesting that Akt can phosphorylate FANCA. We performed in vitro kinase assays using as substrate either a GST-fusion wild-type (WT) FANCA fragment or a GST-fusion FANCA fragment containing a mutation from serine to alanine at 1149 (FANCA-S1149A). These experiments confirmed that FANCA is phosphorylated at Ser 1149, in vitro. However, (32)P-orthophosphate labeling experiments revealed that FANCA-S1149A was more efficiently phosphorylated than WT-FANCA. Furthermore, phosphorylation of wild-type FANCA was blocked by coexpression of a constitutively active (CA)-Akt and enhanced by a dominant-negative (DN) Akt. Our results suggest that Akt is a negative regulator of FANCA phosphorylation.

Pubmed ID: 11855836


  • Otsuki T
  • Nagashima T
  • Komatsu N
  • Kirito K
  • Furukawa Y
  • Kobayashi Si S
  • Liu JM
  • Ozawa K


Biochemical and biophysical research communications

Publication Data

March 1, 2002

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Cell Line
  • Consensus Sequence
  • DNA-Binding Proteins
  • Fanconi Anemia Complementation Group A Protein
  • Genetic Complementation Test
  • Humans
  • Phosphorylation
  • Precipitin Tests
  • Protein-Serine-Threonine Kinases
  • Proteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-akt